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Biochim Biophys Acta. 2003 Jun 26;1649(1):85-96.

Aromatic side-chain interactions in proteins. Near- and far-sequence His-X pairs.

Author information

1
Centre de Biophysique Moléculaire Numérique (CBMN), 2, Passage des déportés, Faculté Scientifique Agronomique de Gembloux (FSAGx), Gembloux 5030, Belgium.

Abstract

Several studies have analysed aromatic interactions, involving mostly phenylalanine, tyrosine and tryptophan. Only a few studies have considered histidine as an interacting aromatic residue. An extensive analysis of aromatic His-X interactions is performed here on a data set of 593 PDB structures: 68% of the histidine are involved in aromatic pairs and 1271 non-redundant His-X pairs were analysed. Thirty percent of these pairs involve an aromatic partner less than 6 apart in the sequence. These near-sequence pairs correspond to conformations which stabilise secondary structures, mainly alpha-helices when the residues are 4 apart and beta-strands when they are 2 apart in the sequence. The partners of the other His-X pairs (887, 70%) are more than 5 apart in the sequence. Of these far-sequence pairs, 35% bridge beta strands and only 9% helices. The near-sequence pairs are sterically constrained as supported by conformer distribution. The X partners of far-sequence His-X pairs are mainly "above" the histidine ring with tilted and normal rings, corresponding to a "T shape; face to edge" orientation. Phenylalanine, the only aromatic residue with no heteroatom, is a disfavoured partner, whereas histidine is the preferred one. Heteroatom-heteroatom interactions are favoured in near-sequence as well as in far-sequence His-His, His-Trp and His-Tyr pairs.

PMID:
12818194
DOI:
10.1016/s1570-9639(03)00161-4
[Indexed for MEDLINE]

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